Sandbox Reserved 1785: Difference between revisions

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=='''Signal Transduction'''==

[[Image:Signal_diagram_2.png|400 px|~~left~~|thumb|'''Figure 4. IgM Antibody Signal Transduction following Antigen Binding.''' The tyrosine residues on the intracellular end of Igα and Igβ helices are phosphorylated by potential tyrosine kinases: Splenic-tyrosine kinase and Src family kinase. Although the exact mechanism is unknown, the phosphorylation of Igα and Igβ activates the B cell and triggers intracellular downstream signaling.]]

[[Image:Signal_diagram_2.png|400 px|right|thumb|'''Figure 4. IgM Antibody Signal Transduction following Antigen Binding.''' The tyrosine residues on the intracellular end of Igα and Igβ helices are phosphorylated by potential tyrosine kinases: Splenic-tyrosine kinase and Src family kinase. Although the exact mechanism is unknown, the phosphorylation of Igα and Igβ activates the B cell and triggers intracellular downstream signaling.]]

<div style="text-align: justify">Based on the structure of IgM, the diagram in Figure 4 depicts the initial process of B cell activation by the antigen binding to the antibody at the Fab region. The underlying mechanism for signal transduction is unknown due to the lack of specificity on which tyrosine residues in the Igα and Igβ domains are phosphorylated, but it is speculated to operate under what is known as the conserved assembly mechanism. <ref name="Ma">PMID:35981028</ref> Following an antigen binding, BCRs on the surface of the cell begin to cluster to cause the phosphorylation of the ITAMs located in Igα and Igβ. In its “off” state, the constant region 4 of heavy chain B <scene name='95/952713/Signal_clustering/2'>overlaps</scene> the extracellular components of Igα and Igβ. The antigen binding induces a conformational change to release the overlap and allow for clustering about the BCR. Now, in its “on” state, the phosphorylation of the [https://en.wikipedia.org/wiki/Immunoreceptor_tyrosine-based_activation_motif ITAM region] within the intracellular tails of Igα and Igβ drives downstream kinase activity. As observed in Figure 4, the activated antibody can now continue to process of [https://en.wikipedia.org/wiki/Tyrosine-protein_kinase_SYK intracellular signal cascading].

Sandbox Reserved 1785: Difference between revisions

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@@ Line 55: / Line 55: @@
 =='''Signal Transduction'''==
-[[Image:Signal_diagram_2.png|400 px|left|thumb|'''Figure 4. IgM Antibody Signal Transduction following Antigen Binding.''' The tyrosine residues on the intracellular end of Igα and Igβ helices are phosphorylated by potential tyrosine kinases: Splenic-tyrosine kinase and Src family kinase. Although the exact mechanism is unknown, the phosphorylation of Igα and Igβ activates the B cell and triggers intracellular downstream signaling.]]
+[[Image:Signal_diagram_2.png|400 px|right|thumb|'''Figure 4. IgM Antibody Signal Transduction following Antigen Binding.''' The tyrosine residues on the intracellular end of Igα and Igβ helices are phosphorylated by potential tyrosine kinases: Splenic-tyrosine kinase and Src family kinase. Although the exact mechanism is unknown, the phosphorylation of Igα and Igβ activates the B cell and triggers intracellular downstream signaling.]]
 <div style="text-align: justify">Based on the structure of IgM, the diagram in Figure 4 depicts the initial process of B cell activation by the antigen binding to the antibody at the Fab region. The underlying mechanism for signal transduction is unknown due to the lack of specificity on which tyrosine residues in the <b><span class="text-brown">Igα</span></b> and <b><span class="text-orange">Igβ</span></b> domains are phosphorylated, but it is speculated to operate under what is known as the conserved assembly mechanism. <ref name="Ma">PMID:35981028</ref> Following an antigen binding, BCRs on the surface of the cell begin to cluster to cause the phosphorylation of the ITAMs located in <b><span class="text-brown">Igα</span></b> and <b><span class="text-orange">Igβ</span></b>. In its “off” state, the constant region 4 of <b><span class="text-blue">heavy chain B</span></b> <scene name='95/952713/Signal_clustering/2'>overlaps</scene> the extracellular components of <b><span class="text-brown">Igα</span></b> and <b><span class="text-orange">Igβ</span></b>. The antigen binding induces a conformational change to release the overlap and allow for clustering about the BCR. Now, in its “on” state, the phosphorylation of the [https://en.wikipedia.org/wiki/Immunoreceptor_tyrosine-based_activation_motif ITAM region] within the intracellular tails of <b><span class="text-brown">Igα</span></b> and <b><span class="text-orange">Igβ</span></b> drives downstream kinase activity. As observed in Figure 4, the activated antibody can now continue to process of [https://en.wikipedia.org/wiki/Tyrosine-protein_kinase_SYK intracellular signal cascading].